Nonclassical binding of formylated peptide in crystal structure of the MHC class lb molecule H2-M3

Chyung Ru Wang, A. Raúl Castaño, Per A. Peterson, Clive Slaughter, Kirsten Fischer Lindahl, Johann Deisenhofer

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Abstract

H2-M3 is a class Ib MHC molecule of the mouse with a 104-fold preference for binding N-fonmylated peptides. To elucidate the basis of this unusual specificity, we expressed and crystallized a soluble form of M3 with a fonnylated nonamer peptide, fMYFINILTL, and determined the structure by X-ray crystallography. M3, refined at 2.1 Å resolution, resembles class la MHC molecules in its overall structure, but differs in the peptide-binding groove. The A pocket, which usually accommodates the free N-terminus of a bound peptide, is closed, and the peptide Is shifted one residue, such that the P1 side chain is lodged in the B pocket. The formyl group Is coordinated by His-9 and a bound water on the floor of the groove.

Original languageEnglish (US)
Pages (from-to)655-664
Number of pages10
JournalCell
Volume82
Issue number4
DOIs
StatePublished - Aug 25 1995

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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    Wang, C. R., Castaño, A. R., Peterson, P. A., Slaughter, C., Fischer Lindahl, K., & Deisenhofer, J. (1995). Nonclassical binding of formylated peptide in crystal structure of the MHC class lb molecule H2-M3. Cell, 82(4), 655-664. https://doi.org/10.1016/0092-8674(95)90037-3